ID   Q8WSE2_9MUSC            Unreviewed;       344 AA.
AC   Q8WSE2;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   SubName: Full=Alpha methyldopa hypersensitive protein {ECO:0000313|EMBL:AAL37911.1};
DE   Flags: Fragment;
GN   Name=amd {ECO:0000313|EMBL:AAL37911.1,
GN   ECO:0000313|FlyBase:FBgn0046970};
OS   Drosophila ellisoni.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=170950 {ECO:0000313|EMBL:AAL37911.1};
RN   [1] {ECO:0000313|EMBL:AAL37911.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Tatarenkov A.N., Ayala F.J.;
RL   Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AAL37911.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=11697926; DOI=10.1006/mpev.2001.1002;
RA   Tatarenkov A., Ayala F.J.;
RT   "Phylogenetic relationships among species groups of the virilis-repleta
RT   radiation of Drosophila.";
RL   Mol. Phylogenet. Evol. 21:327-331(2001).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR602129-50, ECO:0000256|RuleBase:RU000382};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|ARBA:ARBA00009533, ECO:0000256|RuleBase:RU000382}.
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DR   EMBL; AF324953; AAL37911.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8WSE2; -.
DR   FlyBase; FBgn0046970; Dell\amd.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR010977; Aromatic_deC.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   InterPro; IPR021115; Pyridoxal-P_BS.
DR   PANTHER; PTHR11999:SF60; 3,4-DIHYDROXYPHENYLACETALDEHYDE SYNTHASE; 1.
DR   PANTHER; PTHR11999; GROUP II PYRIDOXAL-5-PHOSPHATE DECARBOXYLASE; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   PRINTS; PR00800; YHDCRBOXLASE.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382}.
FT   MOD_RES         220
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAL37911.1"
FT   NON_TER         344
FT                   /evidence="ECO:0000313|EMBL:AAL37911.1"
SQ   SEQUENCE   344 AA;  37997 MW;  BE850140BD122525 CRC64;
     VSYPSIVGEM LASGFSVIGF SWICSPACTE LEVVVMDWLA KFLNLPEHFL HENAGPGGGV
     IQGSASEAVL VAVLAAREQT VRRLRLSQPE LSESEIRGKL IAYSSDQSNS CIEKAGVLAA
     MPIKLLPAGD DLVLRGDALK RAIEQDVAAG LIPVICIASL GTTGTCAYDD IESLASVCEQ
     NEVWLHVDAA YAGGAFALEE CAELRRGLER VDSLNFNLHK FMLVNFDCAA MWLRDANKVI
     DSFNVDRIYL KHKHEGQTQI PDFRHWQIPL GRRFRALKVW ITFRTLGAEG LRAHIRKHIS
     LAAQFEQLVK ADERFELIAP RALGLVCFRA KGENEITSQL LQRL
//